Amelogenin Supra-Molecular Assembly in vitro Compared with the Architecture of the Forming Enamel Matrix

Vol. 181, No. 3-4, 2005

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Paper

Amelogenin Supra-Molecular Assembly in vitro Compared with the Architecture of the Forming Enamel Matrix
Janet Moradian-Oldak^a, Michel Goldberg^b

^aCenter for Craniofacial Molecular Biology, University of Southern California School of Dentistry, Los Angeles, Calif., USA;
^bOral Biology, Faculté de Chirurgie Dentaire, Université Paris V, Montrouge, France

Address of Corresponding Author

Cells Tissues Organs 2005;181:202-218 (DOI: 10.1159/000091382)

Key Words

Biomineralization
Amelogenin
Enamel
Apatite
Macromolecular assembly

Abstract

Tooth enamel is formed in the extracellular space within an organic matrix enriched in amelogenin proteins. Amelogenin nanosphere assembly is a key factor in controlling the oriented and organized growth of enamel apatite crystals. Recently, we have reported the formation of higher ordered structures resulting from organized association and self-orientation of amelogenin nanospheres in vitro. This remarkable hierarchical organization includes self-assembly of amelogenin molecules into subunits of 4-6 nm in diameter followed by their assembly to form nanospheres of 15-25 nm in radii. Chains of >100 nm length are then formed as the result of nanosphere association. These linear arrays of nanospheres assemble to form the microribbons that are hundreds of microns in length, tens of microns in width, and a few microns in thickness. Here, we review the step by step process of amelogenin self-assembly during the formation of microribbon structures in vitro. Assembly properties of selected amelogenins lacking the hydrophilic C terminus will then be reviewed. We will consider amelogenin as a template for the organized growth of crystals in vitro. Finally, we will compare the structures formed in vitro with globular and periodic structures observed earlier, in vivo, by different sample preparation conditions. We propose that the alignment of amelogenin nanospheres into long chains is evident in vivo, and is an important indication for the function of this protein in controlling the oriented and elongated growth of apatite crystals during enamel biomineralization.

Author Contacts

Janet Moradian-Oldak, PhD
Center for Craniofacial Molecular Biology
University of Southern California School of Dentistry
2250 Alcazar St., CSA 103, Los Angeles, CA 90033 (USA)
Tel. +1 323 442 1759, Fax +1 323 442 2981, E-Mail joldak@usc.edu

Article Information

Number of Print Pages : 17
Number of Figures : 7, Number of Tables : 1, Number of References : 112

Medline Abstract (ID 16612086)

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